Crystallization and preliminary X‐ray study of alkaline β‐mannanase from the alkaliphilic Bacillus sp. N16‐5
Acta Crystallographica Section FPeer ReviewedZhao Yueju +52008Journals
The catalytic domain of an alkaline β‐mannanase from the alkaliphilic Bacillus sp. N16‐5 has been expressed and purified. The recombinant enzyme was crystallized using the hanging‐drop vapour‐diffusion method at 298 K. X‐ray diffraction data were collected to 1.6 Å resolution. The crystal belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 59.03, b = 63.31, c = 83.34 Å. Initial phasing was carried out by molecular replacement using the three‐dimensional structure of a mannanase from the alkaliphilic Bacillus sp. JAMB602 as a search model.
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